ID H2TSS5_TAKRU Unreviewed; 1135 AA.
AC H2TSS5; H2TSS2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Sulfatase 1 {ECO:0000313|Ensembl:ENSTRUP00000027733.3};
GN Name=sulf1 {ECO:0000313|Ensembl:ENSTRUP00000027733.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000027733.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000027733.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000027733.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}.
CC Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus,
CC Golgi stack {ECO:0000256|ARBA:ARBA00004348}.
CC -!- SIMILARITY: Belongs to the sulfatase family.
CC {ECO:0000256|ARBA:ARBA00008779}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H2TSS5; -.
DR STRING; 31033.ENSTRUP00000027733; -.
DR Ensembl; ENSTRUT00000027843.3; ENSTRUP00000027733.3; ENSTRUG00000010989.3.
DR GeneTree; ENSGT00940000157544; -.
DR InParanoid; H2TSS5; -.
DR OMA; WKCVNED; -.
DR OrthoDB; 1365192at2759; -.
DR Proteomes; UP000005226; Chromosome 10.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0008015; P:blood circulation; IEA:Ensembl.
DR GO; GO:0010669; P:epithelial structure maintenance; IEA:Ensembl.
DR GO; GO:0048885; P:neuromast deposition; IEA:Ensembl.
DR GO; GO:0048070; P:regulation of developmental pigmentation; IEA:Ensembl.
DR GO; GO:2000290; P:regulation of myotome development; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR CDD; cd16147; G6S; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR024609; Extracellular_sulfatase_C.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR43108:SF1; EXTRACELLULAR SULFATASE SULF-1; 1.
DR PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR Pfam; PF12548; DUF3740; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1135
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025562757"
FT DOMAIN 42..372
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT DOMAIN 530..670
FT /note="Extracellular sulfatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12548"
FT REGION 474..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 635..662
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 474..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 129190 MW; 44F9C6601FC52AA2 CRC64;
MLMVAWLVLL SLEWAPGSLA FITTRAQGLR GRIQRDRRNI RPNIILIMTD DQDVELGSLQ
VMNKTRKIME DGGTTFTNAF VTTPMCCPSR SSMLTGKYVH NHNTYTNNEN CSSPSWQAQH
EPRSFAVYLN NTGYRTGFFG KYLNEYNGSY IPPGWREWVG LIKNSRFYNY TVCRNGYKEK
HGGEYAKDYF TDLITNDSIN FFRISKRMFP HRPVMMVISH AAPHGPEDSA PQYADHFPNA
SQHITPSYNY APNMDKHWIM QYTGPMRPIH MEFTNFLHRK RLQTLMSVDD SVQKVYDMLE
ETGELENTYI IYTADHGYHI GQFGLVKGKS MPYDFDIRVP FFLRGPNVES GAVNPHLVLN
IDLAPTILHI AGLDTPPDMD GKSLLKLLEQ ERTGNRFKPN RKPKVWRDTF LVERGKMLRK
KDDSASTQHT NSLPKYKKVK ETCQQAEFQT PCEQPGQKWH CVEEITGKWR IQKCKGSPKE
SSRKRVRSLR PRSGYDNGER GCDCGEAAFK PSKVERRSHR QLSSGQRYRP RFVHTRPTRS
LSVEFEGQIY DIDLQADDQS GIRRRAISKR HHNAEDPEYD LGSDDGSEEM LGDDTNAVGY
PNSLKVTHKC FILMNDSVRC EREIYQSSRA WKDHKSYVDQ EIETLQDKIK NLREVRGHLK
RTRPEECDCD GKSYYTRGDK NKAERTKNRK DQLHPFKETA QEADGKAQLY NEIRRRKKER
KEKKRQRKGD DCSLPGLTCF THNNDHWQTA PFWSLGPFCA CTSSNNNTYW CLRTINETHN
TLFCEFSTGF LEYFDLNSDP YQLTNAVYTV DRDILNTLHA QLMEMRSCQG YKQCNPRPKG
ADAAHSPYGT DDRVKLPNLT DEEVNWQGLE DLYSINESLY ECRPDSSPSP DNWVNFQKDV
DKMFALRRLF KKFNRTHTFD ESTLAELGSG AGGGGPEEGS GEELVDLATE ARLTTPAPSR
TPPAPPHTAR PAPERKPEPV VNDIPERLSD KPAGPATPSL AASGGGRVLQ SNMWAQLEEM
EGEVFSGNGL MELETHHSNL LRTHSSRQGL LEPGPGPGGE LLGLSPEEED IFQAQGYLPF
SPQTLSPPTT QTSRSTLQAL ARAALAPPSD FEGSGALPPS LQSDTVRQMR RPPGQ
//